Somatic mutation in a cultured mouse myeloma cell affects antigen binding.
The S107 mouse myeloma cell line synthesizes an IgA antibody that binds the hapten phosphocholine and is similar if not identical in its heavy and light chain variable region sequence to the predominant antibody produced by BALB/c mice in response to immunization with phosphocholine. This cell line frequently and spontaneously generates somatic variants producing immunoglobulins with decreased ability to bind antigen. One such variant, S 107.U1, is described here. This variant has a decreased ability to bind phosphocholine when it is attached to a carrier, although its affinity for free hapten is the same as that of the parent. This decrease in antigen binding is associated with a single amino acid substitution at the fifth residue in the JH segment.
D000595:Amino Acid Sequence; D000818:Animals; D000937:Antigen-Antibody Reactions; D001666:Binding Sites, Antibody / Q000235:genetics*; D002460:Cell Line; D006241:Haptens / Q000276:immunology; D007070:Immunoglobulin A / Q000235:genetics* / Q000276:immunology; D007143:Immunoglobulin Heavy Chains / Q000235:genetics*; D007135:Immunoglobulin Variable Region / Q000235:genetics*; D051379:Mice; D009101:Multiple Myeloma; D009154:Mutation; D010767:Phosphorylcholine / Q000276:immunology
D006241:Haptens; D007070:Immunoglobulin A; D007143:Immunoglobulin Heavy Chains; D007135:Immunoglobulin Variable Region; D010767:Phosphorylcholine